Dr Kate Heesom
B.A.(Oxon.), Ph.D.(Bristol)
Expertise
I run the University’s Proteomics Facility, which focuses on the identification of proteins in complex samples and the analysis of changes in protein expression and post-translational modification between different conditions.
Current positions
Senior Research Fellow (Proteomics Facility Director)
Life Sciences Faculty Office
Contact
Press and media
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Research interests
As Director of the University of Bristol Proteomics Facility, I run a core research facility that provides a full range of bespoke proteomics services allowing the isolation, identification and quantitation of proteins of interest for researchers within the University of Bristol and to external academic and industrial clients.
The key services provided by the Facility are:
- Protein identification: we can identify the proteins present in anything from a single gel band up to a total cell lysate or tissue homogenate.
- Quantitative Proteomics (eg. TMT and SILAC) for the analysis of changes in protein levels between different samples or conditions.
- Phospho-Proteomics for the identification of phosphorylated proteins and the analysis of changes in phosphorylation between different samples or conditions.
- Interactome Analysis (eg. AP-MS) for the analysis of protein binding partners.
- Secretome analysis.
- Serum proteomics.
Projects and supervisions
Research projects
Enabling advanced analytics for all users of the proteomics facility
Principal Investigator
Role
Co-Investigator
Managing organisational unit
Bristol Veterinary SchoolDates
01/01/2018 to 08/06/2021
Thesis supervisions
Publications
Recent publications
06/06/2024Harvesting and amplifying gene cassettes confers cross-resistance to critically important antibiotics
PLoS Pathogens
Improving Nitrofurantoin Resistance Prediction in Escherichia coli from Whole Genome Sequence by Integrating NfsA/B Enzyme Assays
Antimicrobial Agents and Chemotherapy
Profiling of insulin-resistant kidney models and human biopsies reveals common and cell-type-specific mechanisms underpinning Diabetic Kidney Disease
Nature Communications
Roles for CEP170 in cilia function and dynein-2 assembly
Journal of Cell Science
Structural basis for coupling of the WASH subunit FAM21 with the endosomal SNX27-Retromer complex
Proceedings of the National Academy of Sciences of the United States of America